Manganese in PDB 4nhk: Crystal Structure of TPA1P From Saccharomyces Cerevisiae, Termination and Polyadenylation Protein 1, in Complex with Pyridine-2,4- Dicarboxylic Acid (2,4-Pdca)

The structure of Crystal Structure of TPA1P From Saccharomyces Cerevisiae, Termination and Polyadenylation Protein 1, in Complex with Pyridine-2,4- Dicarboxylic Acid (2,4-Pdca), PDB code: 4nhk was solved by J.S.Scotti, M.A.Mcdonough, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.63 / 1.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	168.044, 67.716, 70.871, 90.00, 104.93, 90.00
R / Rfree (%)	15.5 / 17.6

The binding sites of Manganese atom in the Crystal Structure of TPA1P From Saccharomyces Cerevisiae, Termination and Polyadenylation Protein 1, in Complex with Pyridine-2,4- Dicarboxylic Acid (2,4-Pdca) (pdb code 4nhk). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of TPA1P From Saccharomyces Cerevisiae, Termination and Polyadenylation Protein 1, in Complex with Pyridine-2,4- Dicarboxylic Acid (2,4-Pdca), PDB code: 4nhk:

Manganese binding site 1 out of 1 in the Crystal Structure of TPA1P From Saccharomyces Cerevisiae, Termination and Polyadenylation Protein 1, in Complex with Pyridine-2,4- Dicarboxylic Acid (2,4-Pdca)


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of TPA1P From Saccharomyces Cerevisiae, Termination and Polyadenylation Protein 1, in Complex with Pyridine-2,4- Dicarboxylic Acid (2,4-Pdca) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn701 b:28.3 occ:1.00 O22 A:PD2702 2.1 28.2 1.0 OD2 A:ASP161 2.1 27.1 1.0 NE2 A:HIS159 2.1 24.9 1.0 O A:HOH801 2.2 28.3 1.0 NE2 A:HIS227 2.2 28.4 1.0 N1 A:PD2702 2.3 29.8 1.0 C21 A:PD2702 2.9 33.7 1.0 C2 A:PD2702 3.0 31.4 1.0 CG A:ASP161 3.0 32.0 1.0 CE1 A:HIS227 3.1 30.7 1.0 CE1 A:HIS159 3.1 31.2 1.0 CD2 A:HIS159 3.1 28.0 1.0 OD1 A:ASP161 3.3 35.7 1.0 CD2 A:HIS227 3.3 27.9 1.0 C6 A:PD2702 3.3 33.7 1.0 OE1 A:GLN242 4.0 42.5 1.0 O21 A:PD2702 4.1 32.5 1.0 O1 A:GOL704 4.2 55.7 1.0 ND1 A:HIS159 4.2 30.5 1.0 ND1 A:HIS227 4.2 25.3 1.0 CG A:HIS159 4.3 26.0 1.0 C3 A:PD2702 4.4 34.4 1.0 CG A:HIS227 4.4 26.2 1.0 CB A:ASP161 4.4 27.2 1.0 C5 A:PD2702 4.6 30.9 1.0 CZ2 A:TRP244 4.7 37.0 1.0 CD A:GLN242 4.7 39.3 1.0 CD2 A:LEU156 4.8 27.2 1.0 O2 A:GOL704 4.8 59.8 1.0 CZ A:PHE218 4.9 27.8 1.0 CA A:ASP161 4.9 30.4 1.0

J.S.Scotti, J.S.Scotti, M.A.Mcdonough, C.J.Schofield. N/A N/A.